ID   AROQ2_RALSO             Reviewed;         154 AA.
AC   Q8XQ89;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=3-dehydroquinate dehydratase 2;
DE            Short=3-dehydroquinase 2;
DE            EC=4.2.1.10;
DE   AltName: Full=Type II DHQase 2;
GN   Name=aroQ2; OrderedLocusNames=RSp1397; ORFNames=RS02061;
OS   Ralstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum).
OG   Plasmid megaplasmid Rsp.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=267608;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GMI1000;
RX   PubMed=11823852; DOI=10.1038/415497a;
RA   Salanoubat M., Genin S., Artiguenave F., Gouzy J., Mangenot S., Arlat M.,
RA   Billault A., Brottier P., Camus J.-C., Cattolico L., Chandler M.,
RA   Choisne N., Claudel-Renard C., Cunnac S., Demange N., Gaspin C., Lavie M.,
RA   Moisan A., Robert C., Saurin W., Schiex T., Siguier P., Thebault P.,
RA   Whalen M., Wincker P., Levy M., Weissenbach J., Boucher C.A.;
RT   "Genome sequence of the plant pathogen Ralstonia solanacearum.";
RL   Nature 415:497-502(2002).
CC   -!- FUNCTION: Catalyzes a trans-dehydration via an enolate intermediate.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O;
CC         Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630,
CC         ChEBI:CHEBI:32364; EC=4.2.1.10;
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC       chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC       3/7.
CC   -!- SUBUNIT: Homododecamer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the type-II 3-dehydroquinase family.
CC       {ECO:0000305}.
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DR   EMBL; AL646053; CAD18548.1; -; Genomic_DNA.
DR   RefSeq; WP_011004647.1; NC_003296.1.
DR   AlphaFoldDB; Q8XQ89; -.
DR   SMR; Q8XQ89; -.
DR   STRING; 267608.RSp1397; -.
DR   EnsemblBacteria; CAD18548; CAD18548; RSp1397.
DR   GeneID; 60504304; -.
DR   KEGG; rso:RSp1397; -.
DR   eggNOG; COG0757; Bacteria.
DR   HOGENOM; CLU_090968_2_0_4; -.
DR   OMA; CAGIVIN; -.
DR   UniPathway; UPA00053; UER00086.
DR   Proteomes; UP000001436; Plasmid megaplasmid Rsp.
DR   GO; GO:0003855; F:3-dehydroquinate dehydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00466; DHQase_II; 1.
DR   Gene3D; 3.40.50.9100; -; 1.
DR   HAMAP; MF_00169; AroQ; 1.
DR   InterPro; IPR001874; DHquinase_II.
DR   InterPro; IPR018509; DHquinase_II_CS.
DR   InterPro; IPR036441; DHquinase_II_sf.
DR   PANTHER; PTHR21272; PTHR21272; 1.
DR   Pfam; PF01220; DHquinase_II; 1.
DR   PIRSF; PIRSF001399; DHquinase_II; 1.
DR   SUPFAM; SSF52304; SSF52304; 1.
DR   TIGRFAMs; TIGR01088; aroQ; 1.
DR   PROSITE; PS01029; DEHYDROQUINASE_II; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Lyase; Plasmid;
KW   Reference proteome.
FT   CHAIN           1..154
FT                   /note="3-dehydroquinate dehydratase 2"
FT                   /id="PRO_0000159924"
FT   ACT_SITE        23
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        105
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         79
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         85
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         92
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         106..107
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         116
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            18
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   154 AA;  16477 MW;  5DFE011400241759 CRC64;
     MTSILVLNGP NLNLLGTREP AVYGHETLAD VERLCREEGE RLGHAVACRQ SNHEGQLIDW
     IHEAGRACVR GELLGIVLNA GALTHTSLAL HDAIKGASVP VIEYHISNVH AREPFRHHSW
     IAPAARAVMA GLGVAGYALA LRALVLVAPP RQAA